Nucleotides contiguous to AUG affect translational initiation

Ganoza, M. Clelia; Fraser, Alan R.; Neilson, Thomas

doi:10.1021/bi00607a011

Cited by 51 publications

(38 citation statements)

References 33 publications

(40 reference statements)

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“…Many native RNAs, however, do possess a triplet ending in A, imrnediately preceding A-U-G (references in [2]). Study of hexamers such as U-U-A-A-U-G and A-A-A-A-U-G showed little variation in ability to complex, but these hexamers were less effective than others [6] in forming an initiation complex. Hexamer U-A-A-A-U-G, on the other hand, proved to be a very poor initiator.…”

Section: Discussionmentioning

confidence: 95%

“…obtained by this method have been shown to possess high activity in protein synthesis in vitro [6,7]. Convenient extension of this synthesis to attach monophosphate groupings to the 3' ends of oligomers is demonstrated in this communication (see Scheme).…”

Section: Scheme the Synthesis Of A-g-g-ap And A-g-g-amentioning

confidence: 89%

“…Examination of some sequences at the 5' and 3' ends of A-U-G indicate that bases at the 5' end of A-U-G have considerable influence on initiation complex formation [6]. Thus, tetramers R-A-U-G (where R is a purine nucleoside) were inefficient in allowing entrance of Met-tRNA whereas the corresponding tetramers of Y-A-U-G composition (where Y is a pyrimidine nucleoside) were very effective [6]. Many native RNAs, however, do possess a triplet ending in A, imrnediately preceding A-U-G (references in [2]).…”

Section: Discussionmentioning

confidence: 99%

“…synthesis [1,2,6,7] and also to code for methionine, valine and leucine residues respectively, when they occur in internal positions of mRNAs.…”

mentioning

confidence: 99%

“…One feature that may be important is the occurrence of bases at the 5' terminus of the RNAs which could conceivably complement with a unique sequence in the 3'-terminal portion of the 16-S RNA of the 30-S ribosomal subunit [l, 2,5]. However, inspection of nucleoside sequences around internal A-U-G codons also shows significant complementarity with the 3' end of 16-S RNA [6].…”

mentioning

confidence: 99%

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Synthesis of Biologically Active Portions of an Intercistronic Region by Use of a New 3′‐Phosphate Incorporation Method to Protect 3′‐OH and Their Binding to Ribosomes

Neilson

Gregoire

Fraser

et al. 1979

European Journal of Biochemistry

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To examine the influence of bases contiguous to a starter codon, a rapid means of assembling biologically active regions corresponding to portions, or to analogues of portions of intercistronic regions is desirable. To do this, a chemical method for the specific insertion of 3′‐monophosphate groups on to chemically synthesized trinucleotides, tetranucleotides and hexanucleotides of defined sequence bearing different bases at the 3′ terminus has been devised. The method involved phosphorylation of blocked oligoribonucleotides synthesized by a phosphotriester method. The deblocked oligoribonucleotides were phosphorylated at the 5′ end with T4‐induced polynucleotide kinase. The products of this kinase reaction served as“donors” in RNA ligase reactions. The [32P]pC‐A‐U‐A‐U‐Gp, [32P]pA‐U‐Gp, [32P]pU‐A‐A, [32P]pA‐G‐G‐Ap, [32P]pC‐U‐U‐Ap and [32P]pU‐C‐C‐Up “donors” were used to synthesize A‐G‐G‐A[32P]pC‐A‐U‐A‐U‐Gp, U‐C‐C‐U[32P]pC‐A‐U‐A‐U‐Gp, U‐A‐A[32P]pA‐U‐G, A‐U‐G[32P]pU‐A‐A, U‐A‐A‐G[32P]pA‐G‐G‐Ap, U‐C‐C‐U[32P]pC‐U‐U‐Ap and A‐U‐U‐C[32P]pU‐C‐C‐Up indicating that the method functions with all bases. A‐U‐Gp, PA‐U‐Gp and pC‐A‐U‐A‐U‐Gp were isolated free of reactants and, along with PA‐U‐G, were all shown to promote the formation of translational initiation complexes. A‐G‐G‐A[32P]pC‐A‐U‐A‐U‐Gp, which corresponds to the 5′‐terminal portion of the intracistronic region of the maturation protein of bacteriophage Qβ, bound more efficiently to Escherichia coli ribosomes than the U‐C‐C‐U[32P]pC‐A‐U‐A‐U‐Gp, [32P]pC‐A‐U‐A‐U‐Gp, [32P]pA‐U‐G‐U‐A‐A or [32P]pU‐A‐A‐A‐U‐G controls. The results suggested that the content and number of residues at the 5′ terminus attached to A‐U‐G affect binding of oligonucleotides to ribosomes; purine nucleosides appear to be more effective than pyrimidine nucleosides in this regard.

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Section: Discussionmentioning

confidence: 95%

Section: Scheme the Synthesis Of A-g-g-ap And A-g-g-amentioning

confidence: 89%

Section: Discussionmentioning

confidence: 99%

“…synthesis [1,2,6,7] and also to code for methionine, valine and leucine residues respectively, when they occur in internal positions of mRNAs.…”

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Synthesis of Biologically Active Portions of an Intercistronic Region by Use of a New 3′‐Phosphate Incorporation Method to Protect 3′‐OH and Their Binding to Ribosomes

Neilson

Gregoire

Fraser

et al. 1979

European Journal of Biochemistry

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Das bakterielle Ribosom: ein programmierbares Enzym

Gassen

1982

Angewandte Chemie

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Die Ribosomen‐abhängige Proteinbiosynthese in Bakterien ist ein komplexer Vorgang, an dem über 150 Komponenten beteiligt sind. Das Ribosom, das aus 53 Proteinen und drei Nucleinsäuren aufgebaut ist, katalysiert als Enzym die Bildung der Peptidbindung. Anders jedoch als konventionelle Enzyme ist das Ribosom durch die mRNA — das Transkript der DNA — „programmierbar”︁. Es entziffert die Nucleotidsequenz der mRNA und setzt sie in die Aminosäuresequenz eines Proteins um. Ähnlich wie bei der Muskelkontraktion wird hierbei chemische Bindungsenergie benutzt, um eine mechanische Bewegung zu ermöglichen. Das hier vorgestellte Modell der Proteinbiosynthese an programmierbaren Ribosomen gibt Antworten auf folgende Fragen: Wie wird die mRNA in Informationseinheiten gerastert, wie wird die Substratspezifität des Ribosoms durch das Codon moduliert und wie bewegt sich die mRNA am Ribosom um ein Trinucleotid pro gebildete Peptidbindung vorwärts?

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The Bacterial Ribosome: A Programmed Enzyme

Gassen

1982

Angew. Chem. Int. Ed. Engl.

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Ribosome-dependent protein synthesis in bacteria represents a complex sequence of reactions involving more than 150 compounds. The ribosome, constructed from 53 individual proteins and 3 nucleic acids, functions as the enzyme which catalyzes peptide bond formation. In contrast to most known enzymes the ribosome is "programmed" by the mRNAthe short-lived transcript of DNA. The ribosome reads the nucleotide message of the mRNA and transforms its information into the amino acid sequence of a protein. In the course of this process, chemical bond energy is converted into directed mechanical motion. The model of protein biosynthesis on the programmable ribosome provides answers to the following questions: how is the mRNA framed into information units, how is the substrate specificity of the ribosome modulated by the codon of the mRNA, and how does the mRNA move with respect to the ribosome by one trinucleotide per peptide bond formed?

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Nucleotides contiguous to AUG affect translational initiation

Cited by 51 publications

References 33 publications

Synthesis of Biologically Active Portions of an Intercistronic Region by Use of a New 3′‐Phosphate Incorporation Method to Protect 3′‐OH and Their Binding to Ribosomes

Synthesis of Biologically Active Portions of an Intercistronic Region by Use of a New 3′‐Phosphate Incorporation Method to Protect 3′‐OH and Their Binding to Ribosomes

Das bakterielle Ribosom: ein programmierbares Enzym

The Bacterial Ribosome: A Programmed Enzyme

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